[HTML][HTML] Ternary complex of transforming growth factor-β1 reveals isoform-specific ligand recognition and receptor recruitment in the superfamily
Transforming growth factor (TGF)-β1,-β2, and-β3 are 25-kDa homodimeric polypeptides that
play crucial nonoverlapping roles in embryogenesis, tissue development, carcinogenesis,
and immune regulation. Here we report the 3.0-Å resolution crystal structure of the ternary
complex between human TGF-β1 and the extracellular domains of its type I and type II
receptors, TβRI and TβRII. The TGF-β1 ternary complex structure is similar to previously
reported TGF-β3 complex except with a 10° rotation in TβRI docking orientation. Quantitative …
play crucial nonoverlapping roles in embryogenesis, tissue development, carcinogenesis,
and immune regulation. Here we report the 3.0-Å resolution crystal structure of the ternary
complex between human TGF-β1 and the extracellular domains of its type I and type II
receptors, TβRI and TβRII. The TGF-β1 ternary complex structure is similar to previously
reported TGF-β3 complex except with a 10° rotation in TβRI docking orientation. Quantitative …